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Volumn 137, Issue 13, 2015, Pages 4300-4303
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Backbone Hydration Determines the Folding Signature of Amino Acid Residues
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Author keywords
[No Author keywords available]
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Indexed keywords
AMINO ACIDS;
AROMATIC COMPOUNDS;
AROMATIZATION;
CHAINS;
HYDROGEN BONDS;
MOLECULAR DYNAMICS;
PEPTIDES;
POLYPEPTIDES;
PROTEINS;
AMINO ACID RESIDUES;
AROMATIC AMINO ACID;
AROMATIC SIDE CHAINS;
AROMATIC SUBSTITUTIONS;
INTERNAL HYDROGEN BONDS;
MOLECULAR DYNAMICS TRAJECTORIES;
RESIDUAL DIPOLAR COUPLINGS;
THREE-DIMENSIONAL STRUCTURE;
HYDRATION;
AROMATIC AMINO ACID;
GLYCINE;
INTRINSICALLY DISORDERED PROTEIN;
TRYPTOPHAN;
TYROSINE;
AMINO ACID;
OLIGOPEPTIDE;
WATER;
ALPHA HELIX;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ARTICLE;
HYDROGEN BOND;
MOLECULAR DYNAMICS;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN SECONDARY STRUCTURE;
PROTON NUCLEAR MAGNETIC RESONANCE;
CHEMISTRY;
AMINO ACID SEQUENCE;
AMINO ACIDS;
HYDROGEN BONDING;
MOLECULAR DYNAMICS SIMULATION;
OLIGOPEPTIDES;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
WATER;
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EID: 84926610746
PISSN: 00027863
EISSN: 15205126
Source Type: Journal
DOI: 10.1021/jacs.5b00660 Document Type: Article |
Times cited : (17)
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References (28)
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